ArticleJournal of molecular biology2016
DHX9/RHA Binding to the PBS-Segment of the Genomic RNA during HIV-1 Assembly Bolsters Virion Infectivity.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Porcine epidemic diarrhea virus suppresses DHX9-mediated antiviral transcription through its nucleocapsid protein.Communications biology · 2026Article
- Incorporation of genome-bound cellular proteins into HIV-1 particles regulates viral infection.Cell reports · 2026Article
- DEAD-box helicase intrinsically disordered domains and structural dynamics of HIV-1 RNA are required to reveal DDX3X catalytic efficiency.Nucleic acids research · 2025Article
- Established and Emerging Roles of DEAD/H-Box Helicases in Regulating Infection and Immunity.Immunological reviews · 2025Review
- Putting a Kink in HIV-1 Particle Infectivity: Rocaglamide Inhibits HIV-1 Replication by Altering Gag-Genomic RNA Interaction.Viruses · 2024Article
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Retroviral PBS-segment sequence and structure: Orchestrating early and late replication events.Retrovirology · 2024Review
- The human cellular protein NoL12 is a specific partner of the HIV-1 nucleocapsid protein NCp7.Journal of virology · 2023Article
- Nucleic DHX9 cooperates with STAT1 to transcribe interferon-stimulated genes.Science advances · 2023Article
- Anomalous HIV-1 RNA, How Cap-Methylation Segregates Viral Transcripts by Form and Function.Viruses · 2022Review
- HIV-1 hypermethylated guanosine cap licenses specialized translation unaffected by mTOR.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DExD/H-box helicases: multifunctional regulators in antiviral innate immunity.Cellular and molecular life sciences : CMLS · 2021Review
- The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity.Nucleic acids research · 2021Article
- MLE Helicase Is a New Participant in the Transcription Regulation of the ftz-f1 Gene Encoding Nuclear Receptor in Higher Eukaryotes.Doklady. Biochemistry and biophysics · 2021Article
- Identification of host proteins differentially associated with HIV-1 RNA splice variants.eLife · 2021Article
- The enigmatic helicase DHX9 and its association with the hallmarks of cancer.Future science OA · 2020Review
- Identification of DHX9 as a cell cycle regulated nucleolar recruitment factor for CIZ1.Scientific reports · 2020Article
- NMR Studies of Retroviral Genome Packaging.Viruses · 2020Review
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8 authors.
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Abstract
Cellular RNA-binding proteins incorporated into virions during human immunodeficiency virus type 1 (HIV-1) assembly promote the replication efficiency of progeny virions. Despite its critical role in bolstering virion infectivity, the molecular basis for the incorporation of DHX9/RNA helicase A (RHA) to virions remains unclear. Here, cell-based experiments demonstrate that the truncation of segments of the HIV-1 5'-untranslated region (5'-UTR) distinct from the core encapsidation sequence eliminated virion incorporation of RHA, indicating that RHA recruitment is mediated by specific interactions with the HIV-1 5'-UTR. In agreement with biological data, isothermal titration calorimetry determined that the dimer conformation of the 5'-UTR binds one RHA molecule per RNA strand, and the interaction is independent of nucleocapsid protein binding. NMR spectra employing a deuterium-labeling approach enabled resolution of the dimeric 5'-UTR in complex with the RHA N-terminal domain. The structure of the large molecular mass complex was dependent on RHA binding to a double-stranded region of the primer binding site (PBS)-segment of the 5'-UTR. A single A-to-C substitution was sufficient to disrupt biophysical conformation and attenuate virion infectivity in cell-based assays. Taken together, our studies demonstrate the structural basis for HIV-1 genomic RNA to recruit beneficial cellular cofactor to virions. The support of progeny virion infectivity by RHA is attributable to structure-dependent binding at the PBS-segment of the HIV-1 5'-UTR during virus assembly.
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